Hyphal orientation of Candida albicans is regulated by a calcium-dependent mechanism

Alexandra Carolyn Brand, S. Shanks, V. M. S. Duncan, M. Yang, Kenneth MacKenzie, Neil Andrew Robert Gow

Research output: Contribution to journalArticlepeer-review

117 Citations (Scopus)

Abstract

Eukaryotic cells from fungal hyphae to neurites that grow by polarized extension must coordinate cell growth and cell orientation to enable them to exhibit growth tropisms and to respond to relevant environmental cues. Such cells generally maintain a tip-high Ca2+ Cytoplasmic gradient, which is correlated with their ability to exhibit polarized tip growth and to respond to growth-directing extracellular signals [1-5]. In yeast and other fungi, the polarisome, exocyst, Ar and Spitzenkbrper protein complexes collectively orchestrate tip growth and cell polarity, but it is not clear whether these molecular complexes also regulate cell orientation or whether they are influenced by cytoplasmic Ca2+ gradients. Hyphae of the human pathogenic fungus Candida albicans reorient their growth axis in response to underlying surface topography (thigmotropism) [6] and imposed electric fields (galvanotropism) [7]. The establishment and maintenance of directional growth in relation to these environmental cues was Ca2+ dependent. Tropisms were attenuated in media containing low Ca2+ or calcium-channel blockers, and in mutants where calcium channels or elements of the calcium signaling pathway were deleted. Therefore galvanotropism and thigmotropism may both be mediated by localized Ca2+ influx at sites of polarized growth via Ca2+ channels that are activated by appropriate environmental signals.

Original languageEnglish
Pages (from-to)347-352
Number of pages5
JournalCurrent Biology
Volume17
Issue number4
Early online date1 Feb 2007
DOIs
Publication statusPublished - 20 Feb 2007

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Keywords

  • saccharomyces-cerevisiae
  • CA2+ influx
  • channel component
  • plasma-membrane
  • electric-field
  • growth
  • yeast
  • differentiation
  • calcineurin
  • MID1

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